1ce2
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ce2.gif|left|200px]] | + | [[Image:1ce2.gif|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION''' | + | {{Structure |
| + | |PDB= 1ce2 |SIZE=350|CAPTION= <scene name='initialview01'>1ce2</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=CO3:CARBONATE ION'>CO3</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1CE2 is a [ | + | 1CE2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE2 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes., Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13. PMID:[http:// | + | Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes., Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10531476 10531476] |
[[Category: Bubalus bubalis]] | [[Category: Bubalus bubalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 26: | Line 35: | ||
[[Category: structure]] | [[Category: structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:09 2008'' |
Revision as of 08:23, 20 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION
Overview
The structure of buffalo lactoferrin has been determined at 303 K. The crystals belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 77.5, b = 91.0, c = 131.5 A and Z = 4. The structure has been refined to an R factor of 0.187. The overall structure of the protein is similar to its structure determined at 277 K in a different crystal form. However, the lobe orientations in the two structures differ by 9.0 degrees, suggesting significant inter-lobe flexibility in this family of proteins. The inter-lobe interactions are predominantly hydrophobic and could act as a cushion for a change in orientation under the influence of external conditions. On the other hand, the domain arrangements are found to be similar in 277 and 303 K crystal structures, with orientations differing by 1.5 and 1.0 degrees in the N and C lobes, respectively. The results of these investigations suggest that the increase in temperature helps in the production of better quality crystals.
About this Structure
1CE2 is a Single protein structure of sequence from Bubalus bubalis. Full crystallographic information is available from OCA.
Reference
Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes., Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13. PMID:10531476
Page seeded by OCA on Thu Mar 20 10:23:09 2008
